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Article: Integrative Chemical Biology Approaches for Identification and Characterization of 'Erasers' for Fatty-Acid-Acylated Lysine Residues within Proteins

TitleIntegrative Chemical Biology Approaches for Identification and Characterization of 'Erasers' for Fatty-Acid-Acylated Lysine Residues within Proteins
Authors
Issue Date2014
Citation
Angewandte Chemie (International Edition), 2014, v. 54 n. 4, p. 1149-1152 How to Cite?
AbstractAcylation of proteins with fatty acids is important for the regulation of membrane association, trafficking, subcellular localization, and activity of many cellular proteins. While significant progress has been made in our understanding of the two major forms of protein acylation with fatty acids, N-myristoylation and S-palmitoylation, studies of the acylation of lysine residues, within proteins, with fatty acids have lagged behind. Demonstrated here is the use of integrative chemical biology approaches to examine human sirtuins as de-fatty-acid acylases in vitro and in cells. Photo-crosslinking chemistry is used to investigate enzymes which recognize fatty-acid acylated lysine. Human Sirt2 was identified as a robust lysine de-fatty-acid acylase in vitro. The results also show that Sirt2 can regulate the acylation of lysine residues, of proteins, with fatty acids within cells.
Persistent Identifierhttp://hdl.handle.net/10722/222462
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorLIU, Z-
dc.contributor.authorYANG, T-
dc.contributor.authorLI, X-
dc.contributor.authorPeng, T-
dc.contributor.authorHang, H-
dc.contributor.authorLi, X-
dc.date.accessioned2016-01-18T07:40:49Z-
dc.date.available2016-01-18T07:40:49Z-
dc.date.issued2014-
dc.identifier.citationAngewandte Chemie (International Edition), 2014, v. 54 n. 4, p. 1149-1152-
dc.identifier.urihttp://hdl.handle.net/10722/222462-
dc.description.abstractAcylation of proteins with fatty acids is important for the regulation of membrane association, trafficking, subcellular localization, and activity of many cellular proteins. While significant progress has been made in our understanding of the two major forms of protein acylation with fatty acids, N-myristoylation and S-palmitoylation, studies of the acylation of lysine residues, within proteins, with fatty acids have lagged behind. Demonstrated here is the use of integrative chemical biology approaches to examine human sirtuins as de-fatty-acid acylases in vitro and in cells. Photo-crosslinking chemistry is used to investigate enzymes which recognize fatty-acid acylated lysine. Human Sirt2 was identified as a robust lysine de-fatty-acid acylase in vitro. The results also show that Sirt2 can regulate the acylation of lysine residues, of proteins, with fatty acids within cells.-
dc.languageeng-
dc.relation.ispartofAngewandte Chemie (International Edition)-
dc.titleIntegrative Chemical Biology Approaches for Identification and Characterization of 'Erasers' for Fatty-Acid-Acylated Lysine Residues within Proteins-
dc.typeArticle-
dc.identifier.emailLi, X: xiangli@hku.hk-
dc.identifier.authorityLi, X=rp01562-
dc.identifier.doi10.1002/anie.201408763-
dc.identifier.pmcidPMC4382910-
dc.identifier.hkuros256645-
dc.identifier.volume54-
dc.identifier.issue4-
dc.identifier.spage1149-
dc.identifier.epage1152-

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